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Details on Person UniProt:P09619 PDGFRB
| Class:Id | ReferenceGeneProduct:61600 |
|---|---|
| _chainChangeLog | signal peptide:1-32 added on Fri February 6 2015;chain:33-1106 added on Fri February 6 2015 |
| _displayName | UniProt:P09619 PDGFRB |
| _timestamp | 2025-08-15 21:25:20 |
| chain | signal peptide:1-32 chain:33-1106 |
| checksum | 038C15E531D6E89D |
| comment | FUNCTION Tyrosine-protein kinase that acts as a cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor.CATALYTIC ACTIVITY L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+)ACTIVITY REGULATION Present in an inactive conformation in the absence of bound ligand. Binding of PDGFB and/or PDGFD leads to dimerization and activation by autophosphorylation on tyrosine residues. Inhibited by imatinib.SUBUNIT Interacts with homodimeric PDGFB and PDGFD, and with heterodimers formed by PDGFA and PDGFB. May also interact with homodimeric PDGFC. Monomer in the absence of bound ligand. Interaction with homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD, leads to receptor dimerization, where both PDGFRA homodimers and heterodimers with PDGFRB are observed. Interacts with SH2B2/APS. Interacts directly (tyrosine phosphorylated) with SHB. Interacts (tyrosine phosphorylated) with PIK3R1 and RASA1. Interacts (tyrosine phosphorylated) with CBL. Interacts (tyrosine phosphorylated) with SRC and SRC family kinases. Interacts (tyrosine phosphorylated) with PIK3C2B, maybe indirectly. Interacts (tyrosine phosphorylated) with SHC1, GRB7, GRB10 and NCK1. Interaction with GRB2 is mediated by SHC1. Interacts (via C-terminus) with NHERF1.INTERACTION After ligand binding, the autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation.ALTERNATIVE PRODUCTS Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-579, and to a lesser degree, at Tyr-581, is important for interaction with SRC family kinases. Phosphorylation at Tyr-740 and Tyr-751 is important for interaction with PIK3R1. Phosphorylation at Tyr-751 is important for interaction with NCK1. Phosphorylation at Tyr-771 and Tyr-857 is important for interaction with RASA1/GAP. Phosphorylation at Tyr-857 is important for efficient phosphorylation of PLCG1 and PTPN11, resulting in increased phosphorylation of AKT1, MAPK1/ERK2 and/or MAPK3/ERK1, PDCD6IP/ALIX and STAM, and in increased cell proliferation. Phosphorylation at Tyr-1009 is important for interaction with PTPN11. Phosphorylation at Tyr-1009 and Tyr-1021 is important for interaction with PLCG1. Phosphorylation at Tyr-1021 is important for interaction with CBL; PLCG1 and CBL compete for the same binding site. Dephosphorylated by PTPRJ at Tyr-751, Tyr-857, Tyr-1009 and Tyr-1021. Dephosphorylated by PTPN2 at Tyr-579 and Tyr-1021.PTM N-glycosylated.PTM Ubiquitinated. After autophosphorylation, the receptor is polyubiquitinated, leading to its degradation.DISEASE A chromosomal aberration involving PDGFRB is found in a form of chronic myelomonocytic leukemia (CMML). Translocation t(5;12)(q33;p13) with EVT6/TEL. It is characterized by abnormal clonal myeloid proliferation and by progression to acute myelogenous leukemia (AML).DISEASE The gene represented in this entry may be involved in disease pathogenesis. Chromosomal aberrations involving PDGFRB have been found in many instances of chronic myeloproliferative disorder with eosinophilia. Translocation t(5;12) with ETV6 on chromosome 12 creating an PDGFRB-ETV6 fusion protein (PubMed:12181402). Translocation t(5;15)(q33;q22) with TP53BP1 creating a PDGFRB-TP53BP1 fusion protein (PubMed:15492236). Translocation t(1;5)(q23;q33) that forms a PDE4DIP-PDGFRB fusion protein (PubMed:12907457). Translocation t(5;6)(q33-34;q23) with CEP85L that fuses the 5'-end of CEP85L (isoform 4) to the 3'-end of PDGFRB (PubMed:21938754).DISEASE The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving PDGFRB has been found in a patient with AML. Translocation t(5;14)(q33;q32) with TRIP11 (PubMed:9373237).DISEASE The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving PDGFRB has been found in a patient with JMML. Translocation t(5;17)(q33;p11.2) with SPECC1 (PubMed:15087372).DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease may be caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily. |
| description | recommendedName: Platelet-derived growth factor receptor beta shortName: PDGF-R-beta shortName: PDGFR-beta ecNumber: 2.7.10.1 alternativeName: Beta platelet-derived growth factor receptor alternativeName: Beta-type platelet-derived growth factor receptor alternativeName: CD140 antigen-like family member B alternativeName: Platelet-derived growth factor receptor 1 shortName: PDGFR-1 cdAntigenNameCD140b/cdAntigenName |
| geneName | PDGFRB PDGFR PDGFR1 |
| identifier | P09619 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Alternative splicing ATP-binding Cell membrane Chemotaxis Chromosomal rearrangement Cytoplasmic vesicle Developmental protein Direct protein sequencing Disease variant Disulfide bond Glycoprotein Immunoglobulin domain Kinase Lysosome Membrane Nucleotide-binding Phosphoprotein Proteomics identification Proto-oncogene Receptor Reference proteome Repeat Signal Transferase Transmembrane Transmembrane helix Tyrosine-protein kinase Ubl conjugation |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9862192] Weiser, Joel, 2024-02-26 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15 |
| name | PDGFRB |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8989136] ENSEMBL:ENSG00000113721 PDGFRB [Homo sapiens] |
| secondaryIdentifier | PGFRB_HUMAN B5A957 Q8N5L4 |
| sequenceLength | 1106 |
| species | [Species:48887] Homo sapiens |
| (isoformParent) | [ReferenceIsoform:8975259] UniProt:P09619-1 PDGFRB [Homo sapiens] [ReferenceIsoform:8975260] UniProt:P09619-2 PDGFRB [Homo sapiens] |
| (referenceEntity) | [EntityWithAccessionedSequence:186767] PDGFRB [plasma membrane] [Homo sapiens] [EntityWithAccessionedSequence:186803] p-12Y-PDGFRB [plasma membrane] [Homo sapiens] [EntityWithAccessionedSequence:8864039] p-11Y-PDGFRB [plasma membrane] [Homo sapiens] |
| (referenceSequence) | [ModifiedResidue:186768] O4'-phospho-L-tyrosine at 740 [ModifiedResidue:186774] O4'-phospho-L-tyrosine at 1021 [ModifiedResidue:186781] O4'-phospho-L-tyrosine at 581 [ModifiedResidue:186788] O4'-phospho-L-tyrosine at 775 [ModifiedResidue:186793] O4'-phospho-L-tyrosine at 771 [ModifiedResidue:186804] O4'-phospho-L-tyrosine at 579 [ModifiedResidue:186807] O4'-phospho-L-tyrosine at 716 [ModifiedResidue:186808] O4'-phospho-L-tyrosine at 778 [ModifiedResidue:186810] O4'-phospho-L-tyrosine at 763 [ModifiedResidue:186814] O4'-phospho-L-tyrosine at 751 |
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No pathways have been reviewed or authored by UniProt:P09619 PDGFRB (61600)
